Molecular dynamics simulation of glycoprotein-glycans of immunoglobulin G and immunoglobulin M.
Glycoprotein-glycans have recently been implicated to play a variety of functional roles. The same glycan chain have been found complexed with proteins of diverse functions. In this article two such glycan chains found attached to Fc regions of immunoglobulin G and immunoglobulin M have been studied. An extensive simulated annealing procedure have been adopted to arrive at a low-energy minimum of the two oligosaccharides. Molecular dynamics simulations have been performed to study the flexibility of the glycosidic linkages. It was found that both glycan chains can undergo conformational transitions and adopt folded and extended conformations. The two beta (1-2) linkages of complex-type glycan had been found to prefer different conformational regime and the terminal fucose linked to the GlcNAc residue drastically modifies the GlcNAc beta (1-4) GlcNAc linkage conformation. In the high-mannose type glycan chain alpha (1-3) linkages can induce flexibility in addition to the alpha (1-6) linkages. The results have been compared with recent experimental nmr and fluorescence energy transfer data.
Mukhopadhyay
C
C
Distributed Information Center, Bose Institute, Calcutta, India.
D002240:Carbohydrate Sequence; D003198:Computer Simulation; D005643:Fucose / Q000737:chemistry; D006860:Hydrogen Bonding; D007074:Immunoglobulin G / Q000737:chemistry*; D007075:Immunoglobulin M / Q000737:chemistry*; D008358:Mannose / Q000737:chemistry; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011509:Proteoglycans / Q000737:chemistry*
D007074:Immunoglobulin G; D007075:Immunoglobulin M; D011509:Proteoglycans; D005643:Fucose; D008358:Mannose